Dr. Ray has over 15 years of research experience in the field of cancer cell signaling with specific emphasis on understanding the role of post-translational protein modifications during oncogenesis. His research goal involves in identifying ubiquitination machineries involved in the maintenance of oncoproteins’ stabilities including epidermal growth factor receptor (EGFR) and mutant KRAS. He seeks to then further translate such findings to develop novel and efficacious anticancer strategies.
Dr. Ray also has a research interest in understanding the roles of Tumor Necrosis Factor (TNF-α) in radiation pneumonitis and using that to develop a strategy of lung radioprotection. In addition, he has several intra-institutional collaborative projects including one with Dr. David Beer in the Department of Surgery, whose laboratory is studying the novel role of RNF128/Grail, a RING-family ubiquitin ligase (E3) in mutant TP53 protein stability during Barrett’s progression. Another recent collaboration is with Dr. Nithya Ramnath from the Department of Internal Medicine. Her lab is exploring the roles of Vitamin D in metabolizing Cytochrome P450 (CYP24A1), nuclear division, and mitochondrial biogenesis which is critical for lung tumor growth and invasion.
Areas of Interest
- Targeting ubiquitination machinery to destabilize oncoprotein’s stability.
- Lung radioprotection by inhibition of TNF-α signaling.
- 1R01CA160981, (PI: Ray), 9/01/2011-07/31/2017, National Institutes of Health: Targeting SMURF2 as a novel therapy for EGFR-driven tumors, Role: Principal Investigator.
Selected from 35 publications
- Krishnamurthy PM, Shukla S, Ray P, Mehra R, Nyati MK, Lawrence TS, Ray D. Involvement of p38-β-TrCP-Tristetraprolin-TNF-α axis in radiation pneumonitis. Oncotarget, (In press), 2017.
- Shukla, S, Allam US, Ahsan, A, Chen G, Krishnamurthy P M, Marsh, K, Rumschlag M, Shankar S, Whitehead C, Schipper M, Basrur V, Southworth DR, Chinnaiyan AM, Rehemtulla A, Beer D G, Lawrence TS, Nyati MK, and Ray D. KRAS protein stability Is regulated through SMURF2: UBCH5 complex-mediated beta-TrCP1 degradation. Neoplasia, 16: 115-IN115, 2014. PMCID PMC3978392.
- Ray D, Shukla S, Allam US, Helman A, Ramanand SG, Tran L, Bassetti, M, Krishnamurthy PM, Rumschlag M, Paulsen M, Sun L, Shanley TP, Ljungman M, Nyati MK, Zhang M, Lawrence TS. Tristetraprolin mediates radiation-induced TNF-a production in lung macrophages. Plos One, 8(2): e57290, 2013. PMCID PMC3585360.
- Ray D, Ahsan A, Helman A, Chen G, Hegde A, Gurjar SR, Zhao L, Kiyokawa H, Beer DG, Lawrence TS, Nyati MK. Regulation of EGFR protein stability by the HECT-type ubiquitin ligase SMURF2. Neoplasia 13(7): 570-8, 2011. PMCID PMC3132843.
- Osmundson EC, Ray D, Moore F, Gao Q, Thomsen GH, Kiyokawa H. The HECT-domain E3 ligase is required for Mad2-dependent spindle assembly checkpoint and mitotic progression. J Cell Biol 183(2):267-77, 2008. PMCID PMC2568023.